Leucine-rich nuclear-export signals: born to be weak.

Kutay U; Güttinger S

doi:10.1016/j.tcb.2005.01.005

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Journal article

Leucine-rich nuclear-export signals: born to be weak.

Kutay U Swiss Federal Institute of Technology (ETH) Zürich, Institute of Biochemistry, Schafmattstrasse 18, HPM F11.1, 8093 Zürich, Switzerland. ulrike.kutay@bc.biol.ethz.ch
Güttinger S

2005-03-09

Published in:

Trends in cell biology. - 2005

Active Transport, Cell Nucleus

Receptors, Cytoplasmic and Nuclear

English CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.

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